Conservation of the active site motif in Aspergillus niger (ficuum) pH 6.0 optimum acid phosphatase and kidney bean purple acid phosphatase.
Aspergillus niger (ficuum) and the kidney bean purple acid phosphatases retained all the essential amino acids in the active site despite a low degree of total sequence homology. This high degree of homology in the sequence motif of A. niger fungal acid phosphatase (Apase6) active site with Kidney bean metallo phosphoesterase (KBPAP) and the absence of the RHG-XRXP sequence motif indicates Apase6 to be a metallophosphoesterase rather than a histidine acid phosphatase.
Mullaney
E J
EJ
Southern Regional Research Center, ARS, USDA, New Orleans, Louisiana 70124, USA. emul@nola.srrc.usda.gov
Ullah
A H
AH
D010832:6-Phytase / Q000737:chemistry / Q000378:metabolism; D000135:Acid Phosphatase / Q000737:chemistry*; D000595:Amino Acid Sequence; D001233:Aspergillus nidulans / Q000201:enzymology; D001234:Aspergillus niger / Q000201:enzymology*; D001665:Binding Sites / Q000235:genetics; D017124:Conserved Sequence / Q000235:genetics*; D007887:Fabaceae / Q000201:enzymology*; D005656:Fungal Proteins / Q000737:chemistry; D006023:Glycoproteins / Q000737:chemistry*; D008667:Metalloproteins / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry; D010946:Plants, Medicinal; D016415:Sequence Alignment
D005656:Fungal Proteins; D006023:Glycoproteins; D008667:Metalloproteins; D010940:Plant Proteins; C091137:purple acid phosphatase; D000135:Acid Phosphatase; D010832:6-Phytase